ID A0A0R1YRJ3_9LACO Unreviewed; 330 AA.
AC A0A0R1YRJ3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Phosphate acetyltransferase {ECO:0000256|ARBA:ARBA00021528};
DE EC=2.3.1.8 {ECO:0000256|ARBA:ARBA00012707};
DE AltName: Full=Phosphotransacetylase {ECO:0000256|ARBA:ARBA00031108};
GN ORFNames=FD40_GL000395 {ECO:0000313|EMBL:KRM42603.1};
OS Amylolactobacillus amylophilus DSM 20533 = JCM 1125.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Amylolactobacillus.
OX NCBI_TaxID=1423721 {ECO:0000313|EMBL:KRM42603.1, ECO:0000313|Proteomes:UP000051230};
RN [1] {ECO:0000313|EMBL:KRM42603.1, ECO:0000313|Proteomes:UP000051230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20533 {ECO:0000313|EMBL:KRM42603.1,
RC ECO:0000313|Proteomes:UP000051230};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + phosphate = acetyl phosphate + CoA;
CC Xref=Rhea:RHEA:19521, ChEBI:CHEBI:22191, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000705};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 2/2. {ECO:0000256|ARBA:ARBA00004989}.
CC -!- SIMILARITY: Belongs to the phosphate acetyltransferase and
CC butyryltransferase family. {ECO:0000256|ARBA:ARBA00005656}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRM42603.1}.
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DR EMBL; AYYS01000009; KRM42603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1YRJ3; -.
DR STRING; 1423721.LA20533_06875; -.
DR PATRIC; fig|1423721.4.peg.399; -.
DR Proteomes; UP000051230; Unassembled WGS sequence.
DR GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR InterPro; IPR012147; P_Ac_Bu_trans.
DR InterPro; IPR004614; P_AcTrfase.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR002505; PTA_PTB.
DR NCBIfam; TIGR00651; pta; 1.
DR PANTHER; PTHR43356; PHOSPHATE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR43356:SF3; PHOSPHATE ACETYLTRANSFERASE; 1.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF000428; P_Ac_trans; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Reference proteome {ECO:0000313|Proteomes:UP000051230};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..325
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 330 AA; 35797 MW; 2A6100EEA3009C08 CRC64;
MTKESKSMNL FVSLTNKIKG KNLSVVFPEA TDTRVLGAAV RLAQDELLRP VLLGDPTEIK
RVADEKNFDL NSSEIIDPNN YADYEAMVAA FVERRKGKAT KEQAETILRD ETYFGTMLVY
MDKADCLVSG AVHSTANTVR PALQIIKTKP GMTRTSGAFI MQRGDERYLF ADCAININPN
AQELAEIAVQ SAKSAELFGI EPIVGLLSFS TKGSAKSEEV EKVAEATKIA HELAPDLQLD
GELQFDASFV PSVAAQKAPD SKVAGNVKVF VFPELQSGNI GYKIAQRFGN FEAIGPVLQG
LNKPVSDLSR GANEEDVYKT AILTAAQALD
//
